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β-内酰胺类药物对沙眼衣原体青霉素结合蛋白的亲和力及其抗衣原体活性。

Affinities of beta-lactams for penicillin binding proteins of Chlamydia trachomatis and their antichlamydial activities.

作者信息

Storey C, Chopra I

机构信息

Division of Microbiology and Antimicrobial Research Centre, University of Leeds, Leeds LS2 9JT, United Kingdom.

出版信息

Antimicrob Agents Chemother. 2001 Jan;45(1):303-5. doi: 10.1128/AAC.45.1.303-305.2001.

DOI:10.1128/AAC.45.1.303-305.2001
PMID:11120983
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC90278/
Abstract

Binding affinities of beta-lactam antibiotics for the three penicillin binding proteins (PBPs) from Chlamydia trachomatis were determined in vitro and compared with their antichlamydial activities. Mecillinam selectively inhibited PBP1, with a 50% inhibitory concentration for PBP1 binding (0.2 microg/ml) similar to the MIC (0.1 microg/ml) and minimum bactericidal concentration (0.25 microg/ml). Although the other beta-lactams inhibited a wider range of PBPs than mecillinam, their antichlamydial activities were inferior to that of mecillinam.

摘要

在体外测定了β-内酰胺类抗生素对沙眼衣原体三种青霉素结合蛋白（PBPs）的结合亲和力，并将其与它们的抗衣原体活性进行了比较。美西林选择性抑制PBP1，其对PBP1结合的50%抑制浓度（0.2微克/毫升）与最低抑菌浓度（0.1微克/毫升）和最低杀菌浓度（0.25微克/毫升）相似。尽管其他β-内酰胺类抗生素比美西林抑制的PBPs范围更广，但其抗衣原体活性却不如美西林。

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本文引用的文献

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Lack of cell wall peptidoglycan versus penicillin sensitivity: new insights into the chlamydial anomaly.缺乏细胞壁肽聚糖与青霉素敏感性：衣原体异常的新见解
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